4PUT
Crystal structure of the Arabidopsis thaliana TOP2 oligopeptidase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X29A |
Synchrotron site | NSLS |
Beamline | X29A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2013-05-02 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 168.740, 168.740, 175.590 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 48.090 - 3.000 |
R-factor | 0.207 |
Rwork | 0.207 |
R-free | 0.24700 |
Structure solution method | MR |
RMSD bond length | 0.018 |
RMSD bond angle | 1.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PRIME-X |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.110 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.086 | 0.514 |
Number of reflections | 29598 | |
<I/σ(I)> | 13.4 | 2.5 |
Completeness [%] | 98.0 | 97.1 |
Redundancy | 4.5 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 220 mM ammonium acetate and 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |